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Conserved domains on  [gi|966352543|ref|WP_058401040|]
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MULTISPECIES: bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH [Pseudomonas]

Protein Classification

bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH( domain architecture ID 10014284)

bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH catalyzes both the dephosphorylation of phosphoserine (P-Ser) and phosphothreonine (P-Thr), and the transfer of a phosphoryl group to homoserine using phosphoserine as the phosphoryl group donor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
thrH PRK13582
bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH;
1-205 1.20e-151

bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH;


:

Pssm-ID: 237437 [Multi-domain]  Cd Length: 205  Bit Score: 418.56  E-value: 1.20e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352543   1 MEIACLDLEGVLVPEIWIAFAEKTGIESLRATTRDIPDYDVLMKQRLRILDEHGLKLSDIQEVIATLKPLEGAVEFVNWL 80
Cdd:PRK13582   1 MEIVCLDLEGVLVPEIWIAFAEKTGIPELRATTRDIPDYDVLMKQRLDILDEHGLGLADIQEVIATLDPLPGAVEFLDWL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352543  81 RERFQVVILSDTFYEFSQPLMRQLGFPTLLCHRLITDETGRVVSYQLRQKDPKRQSVLAFKSLYYRIIAAGDSYNDTTML 160
Cdd:PRK13582  81 RERFQVVILSDTFYEFAGPLMRQLGWPTLFCHSLEVDEDGMITGYDLRQPDGKRQAVKALKSLGYRVIAAGDSYNDTTML 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 966352543 161 GEADAGILFHAPDNVIREFPQFPAVHTFDELKKEFIKASNRDLPL 205
Cdd:PRK13582 161 GEADAGILFRPPANVIAEFPQFPAVHTYDELLAAIDKASARALSL 205
 
Name Accession Description Interval E-value
thrH PRK13582
bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH;
1-205 1.20e-151

bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH;


Pssm-ID: 237437 [Multi-domain]  Cd Length: 205  Bit Score: 418.56  E-value: 1.20e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352543   1 MEIACLDLEGVLVPEIWIAFAEKTGIESLRATTRDIPDYDVLMKQRLRILDEHGLKLSDIQEVIATLKPLEGAVEFVNWL 80
Cdd:PRK13582   1 MEIVCLDLEGVLVPEIWIAFAEKTGIPELRATTRDIPDYDVLMKQRLDILDEHGLGLADIQEVIATLDPLPGAVEFLDWL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352543  81 RERFQVVILSDTFYEFSQPLMRQLGFPTLLCHRLITDETGRVVSYQLRQKDPKRQSVLAFKSLYYRIIAAGDSYNDTTML 160
Cdd:PRK13582  81 RERFQVVILSDTFYEFAGPLMRQLGWPTLFCHSLEVDEDGMITGYDLRQPDGKRQAVKALKSLGYRVIAAGDSYNDTTML 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 966352543 161 GEADAGILFHAPDNVIREFPQFPAVHTFDELKKEFIKASNRDLPL 205
Cdd:PRK13582 161 GEADAGILFRPPANVIAEFPQFPAVHTYDELLAAIDKASARALSL 205
HSK-PSP TIGR02137
phosphoserine phosphatase/homoserine phosphotransferase bifunctional protein; This protein is ...
 1-203 3.99e-131

phosphoserine phosphatase/homoserine phosphotransferase bifunctional protein; This protein is has been characterized as both a phosphoserine phosphatase and a phosphoserine:homoserine phosphotransferase. In Pseudomonas aeruginosa, where the characterization was done, a second phosphoserine phosphatase (SerB) and a second homoserine kinase (thrB) are found, but in Fibrobacter succinogenes neither are present. This enzyme is a member of the haloacid dehalogenase (HAD) superfamily, specifically part of subfamily IB by virtue of the presence of an alpha helical domain in between motifs I and II of the HAD domain. The closest homologs to this family are monofunctional phosphoserine phosphatases (TIGR00338).


Pssm-ID: 162723  Cd Length: 203  Bit Score: 366.56  E-value: 3.99e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352543    1 MEIACLDLEGVLVPEIWIAFAEKTGIESLRATTRDIPDYDVLMKQRLRILDEHGLKLSDIQEVIATLKPLEGAVEFVNWL 80
Cdd:TIGR02137   1 MEIACLDLEGVLVPEIWIAFAEKTGIDALKATTRDIPDYDVLMKQRLRILDEHGLKLGDIQEVIATLKPLEGAVEFVDWL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352543   81 RERFQVVILSDTFYEFSQPLMRQLGFPTLLCHRLITDETGRVVSYQLRQKDPKRQSVLAFKSLYYRIIAAGDSYNDTTML 160
Cdd:TIGR02137  81 RERFQVVILSDTFYEFSQPLMRQLGFPTLLCHKLEIDDSDRVVGYQLRQKDPKRQSVIAFKSLYYRVIAAGDSYNDTTML 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 966352543  161 GEADAGILFHAPDNVIREFPQFPAVHTFDELKKEFIKASNRDL 203
Cdd:TIGR02137 161 SEAHAGILFHAPENVIREFPQFPAVHTYEDLKREFLKASSRSL 203
HAD_ThrH_like cd02607
bifunctional phosphoserine phosphatase/phosphoserine:homoserine phosphotransferase, similar to ...
 1-195 7.45e-114

bifunctional phosphoserine phosphatase/phosphoserine:homoserine phosphotransferase, similar to Pseudomonas aeruginosa ThrH; This family includes Pseudomonas aeruginosa ThrH which is a duel activity enzyme having both phosphoserine phosphatase and phosphoserine:homoserine phosphotransferase activities, i.e. it can dephosphorylate phosphoserine, and can transfer phosphate from phosphoserine to homoserine. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319793 [Multi-domain]  Cd Length: 195  Bit Score: 322.69  E-value: 7.45e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352543   1 MEIACLDLEGVLVPEIWIAFAEKTGIESLRATTRDIPDYDVLMKQRLRILDEHGLKLSDIQEVIATLKPLEGAVEFVNWL 80
Cdd:cd02607    1 MEIACLDLEGVLVPEIWIAFAEKTGIDALKATTRDIPDYDVLMKQRLRILDEHGLKLADIQEVIATLKPLEGAVEFVDWL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352543  81 RERFQVVILSDTFYEFSQPLMRQLGFPTLLCHRLITDETGRVVSYQLRQKDPKRQSVLAFKSLYYRIIAAGDSYNDTTML 160
Cdd:cd02607   81 RERFQVVILSDTFYEFSQPLMRQLGFPTLLCHKLQTDDDDRVVGYQLRQKDPKRQSVIAVKSLYYRVIAAGDSYNDTTML 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 966352543 161 GEADAGILFHAPDNVIREFPQFPAVHTFDELKKEF 195
Cdd:cd02607  161 SEAHAGILFHAPENVIREFPQFPAVHTYEDLKAEF 195
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 1-178 1.06e-18

Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 440326 [Multi-domain]  Cd Length: 221  Bit Score: 80.27  E-value: 1.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352543   1 MEIACLDLEGVLVPE----IWIAFAEKTGIESLRATTRDIP-----------DYDVLMKQRLRILdeHGLKLSDIQEVIA 65
Cdd:COG0560    3 MRLAVFDLDGTLIAGesidELARFLGRRGLVDRREVLEEVAaiteramagelDFEESLRFRVALL--AGLPEEELEELAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352543  66 TLKP-----LEGAVEFVNWLRER-FQVVILSDTFYEFSQPLMRQLGFPTLLCHRLITDE---TGRVVSYQLRQKDpKRQS 136
Cdd:COG0560   81 RLFEevprlYPGARELIAEHRAAgHKVAIVSGGFTFFVEPIAERLGIDHVIANELEVEDgrlTGEVVGPIVDGEG-KAEA 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 966352543 137 VLAFKSLYY----RIIAAGDSYNDTTMLGEADAGILFHaPDNVIRE 178
Cdd:COG0560  160 LRELAAELGidleQSYAYGDSANDLPMLEAAGLPVAVN-PDPALRE 204
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 13-164 9.25e-08

haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha/beta hydrolase family (pfam00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain. Those members with the characteriztic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria.


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 50.28  E-value: 9.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352543   13 VPEIWIAFAEKTGIESLRATTRDIPDYDVLMKQRLRILDEHGLKLSDIQEVIATLKPLEGAVEFVNWLRER-FQVVILSD 91
Cdd:pfam00702  43 LPIPVEDFTARLLLGKRDWLEELDILRGLVETLEAEGLTVVLVELLGVIALADELKLYPGAAEALKALKERgIKVAILTG 122

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966352543   92 TFYEFSQPLMRQLGFPTLLCHRLITDETGRvvsyqlrqKDPKRQSVLA----FKSLYYRIIAAGDSYNDTTMLGEAD 164
Cdd:pfam00702 123 DNPEAAEALLRLLGLDDYFDVVISGDDVGV--------GKPKPEIYLAalerLGVKPEEVLMVGDGVNDIPAAKAAG 191
 
Name Accession Description Interval E-value
thrH PRK13582
bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH;
1-205 1.20e-151

bifunctional phosphoserine phosphatase/homoserine phosphotransferase ThrH;


Pssm-ID: 237437 [Multi-domain]  Cd Length: 205  Bit Score: 418.56  E-value: 1.20e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352543   1 MEIACLDLEGVLVPEIWIAFAEKTGIESLRATTRDIPDYDVLMKQRLRILDEHGLKLSDIQEVIATLKPLEGAVEFVNWL 80
Cdd:PRK13582   1 MEIVCLDLEGVLVPEIWIAFAEKTGIPELRATTRDIPDYDVLMKQRLDILDEHGLGLADIQEVIATLDPLPGAVEFLDWL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352543  81 RERFQVVILSDTFYEFSQPLMRQLGFPTLLCHRLITDETGRVVSYQLRQKDPKRQSVLAFKSLYYRIIAAGDSYNDTTML 160
Cdd:PRK13582  81 RERFQVVILSDTFYEFAGPLMRQLGWPTLFCHSLEVDEDGMITGYDLRQPDGKRQAVKALKSLGYRVIAAGDSYNDTTML 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 966352543 161 GEADAGILFHAPDNVIREFPQFPAVHTFDELKKEFIKASNRDLPL 205
Cdd:PRK13582 161 GEADAGILFRPPANVIAEFPQFPAVHTYDELLAAIDKASARALSL 205
HSK-PSP TIGR02137
phosphoserine phosphatase/homoserine phosphotransferase bifunctional protein; This protein is ...
 1-203 3.99e-131

phosphoserine phosphatase/homoserine phosphotransferase bifunctional protein; This protein is has been characterized as both a phosphoserine phosphatase and a phosphoserine:homoserine phosphotransferase. In Pseudomonas aeruginosa, where the characterization was done, a second phosphoserine phosphatase (SerB) and a second homoserine kinase (thrB) are found, but in Fibrobacter succinogenes neither are present. This enzyme is a member of the haloacid dehalogenase (HAD) superfamily, specifically part of subfamily IB by virtue of the presence of an alpha helical domain in between motifs I and II of the HAD domain. The closest homologs to this family are monofunctional phosphoserine phosphatases (TIGR00338).


Pssm-ID: 162723  Cd Length: 203  Bit Score: 366.56  E-value: 3.99e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352543    1 MEIACLDLEGVLVPEIWIAFAEKTGIESLRATTRDIPDYDVLMKQRLRILDEHGLKLSDIQEVIATLKPLEGAVEFVNWL 80
Cdd:TIGR02137   1 MEIACLDLEGVLVPEIWIAFAEKTGIDALKATTRDIPDYDVLMKQRLRILDEHGLKLGDIQEVIATLKPLEGAVEFVDWL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352543   81 RERFQVVILSDTFYEFSQPLMRQLGFPTLLCHRLITDETGRVVSYQLRQKDPKRQSVLAFKSLYYRIIAAGDSYNDTTML 160
Cdd:TIGR02137  81 RERFQVVILSDTFYEFSQPLMRQLGFPTLLCHKLEIDDSDRVVGYQLRQKDPKRQSVIAFKSLYYRVIAAGDSYNDTTML 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 966352543  161 GEADAGILFHAPDNVIREFPQFPAVHTFDELKKEFIKASNRDL 203
Cdd:TIGR02137 161 SEAHAGILFHAPENVIREFPQFPAVHTYEDLKREFLKASSRSL 203
HAD_ThrH_like cd02607
bifunctional phosphoserine phosphatase/phosphoserine:homoserine phosphotransferase, similar to ...
 1-195 7.45e-114

bifunctional phosphoserine phosphatase/phosphoserine:homoserine phosphotransferase, similar to Pseudomonas aeruginosa ThrH; This family includes Pseudomonas aeruginosa ThrH which is a duel activity enzyme having both phosphoserine phosphatase and phosphoserine:homoserine phosphotransferase activities, i.e. it can dephosphorylate phosphoserine, and can transfer phosphate from phosphoserine to homoserine. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319793 [Multi-domain]  Cd Length: 195  Bit Score: 322.69  E-value: 7.45e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352543   1 MEIACLDLEGVLVPEIWIAFAEKTGIESLRATTRDIPDYDVLMKQRLRILDEHGLKLSDIQEVIATLKPLEGAVEFVNWL 80
Cdd:cd02607    1 MEIACLDLEGVLVPEIWIAFAEKTGIDALKATTRDIPDYDVLMKQRLRILDEHGLKLADIQEVIATLKPLEGAVEFVDWL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352543  81 RERFQVVILSDTFYEFSQPLMRQLGFPTLLCHRLITDETGRVVSYQLRQKDPKRQSVLAFKSLYYRIIAAGDSYNDTTML 160
Cdd:cd02607   81 RERFQVVILSDTFYEFSQPLMRQLGFPTLLCHKLQTDDDDRVVGYQLRQKDPKRQSVIAVKSLYYRVIAAGDSYNDTTML 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 966352543 161 GEADAGILFHAPDNVIREFPQFPAVHTFDELKKEF 195
Cdd:cd02607  161 SEAHAGILFHAPENVIREFPQFPAVHTYEDLKAEF 195
SerB COG0560
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ...
 1-178 1.06e-18

Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 440326 [Multi-domain]  Cd Length: 221  Bit Score: 80.27  E-value: 1.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352543   1 MEIACLDLEGVLVPE----IWIAFAEKTGIESLRATTRDIP-----------DYDVLMKQRLRILdeHGLKLSDIQEVIA 65
Cdd:COG0560    3 MRLAVFDLDGTLIAGesidELARFLGRRGLVDRREVLEEVAaiteramagelDFEESLRFRVALL--AGLPEEELEELAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352543  66 TLKP-----LEGAVEFVNWLRER-FQVVILSDTFYEFSQPLMRQLGFPTLLCHRLITDE---TGRVVSYQLRQKDpKRQS 136
Cdd:COG0560   81 RLFEevprlYPGARELIAEHRAAgHKVAIVSGGFTFFVEPIAERLGIDHVIANELEVEDgrlTGEVVGPIVDGEG-KAEA 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 966352543 137 VLAFKSLYY----RIIAAGDSYNDTTMLGEADAGILFHaPDNVIRE 178
Cdd:COG0560  160 LRELAAELGidleQSYAYGDSANDLPMLEAAGLPVAVN-PDPALRE 204
HAD_PSP cd07500
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ...
 38-171 7.54e-13

phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces cerevisiae SER2p; This family includes Methanococcus jannaschii PSP, and Saccharomyces cerevisiae phosphoserine phosphatase SER2p, EC 3.1.3.3, which participates in a pathway whereby serine and glycine are synthesized from the glycolytic intermediate 3-phosphoglycerate; phosphoserine phosphatase catalyzes the hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, the third reaction in this pathway. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319803 [Multi-domain]  Cd Length: 180  Bit Score: 64.11  E-value: 7.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352543  38 DYDVLMKQRLRILDehGLKLSDIQEVIATLKPLEGAVEFVNWLRER-FQVVILSDTFYEFSQPLMRQLGFPTLLCHRLIT 116
Cdd:cd07500   42 DFEESLRERVALLK--GLPESVLDEVYERLTLTPGAEELIQTLKAKgYKTAVVSGGFTYFTDRLAEELGLDYAFANELEI 119

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966352543 117 DE---TGRVVSyQLRQKDPKRQSVLAFKSLY----YRIIAAGDSYNDTTMLGEADAGILFHA 171
Cdd:cd07500  120 KDgklTGKVLG-PIVDAQRKAETLQELAARLgiplEQTVAVGDGANDLPMLKAAGLGIAFHA 180
HAD-SF-IB TIGR01488
Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model ...
 3-160 7.39e-11

Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; This model represents a subfamily of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. Subfamily IA, B, C and D are distinguished from the rest of the superfamily by the presence of a variable domain between the first and second conserved catalytic motifs. In subfamilies IA and IB, this domain consists of an alpha-helical bundle. It was necessary to model these two subfamilies separately, breaking them at a an apparent phylogenetic bifurcation, so that the resulting model(s) are not so broadly defined that members of subfamily III (which lack the variable domain) are included. Subfamily IA includes the enzyme phosphoserine phosphatase (TIGR00338) as well as three hypothetical equivalogs. Many members of these hypothetical equivalogs have been annotated as PSPase-like or PSPase-family proteins. In particular, the hypothetical equivalog which appears to be most closely related to PSPase contains only Archaea (while TIGR00338 contains only eukaryotes and bacteria) of which some are annotated as PSPases. Although this is a reasonable conjecture, none of these sequences has sufficient evidence for this assignment. If such should be found, this model should be retired while the PSPase model should be broadened to include these sequences. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273653 [Multi-domain]  Cd Length: 177  Bit Score: 58.52  E-value: 7.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352543    3 IACLDLEGVLVPE--IWIAFAEKTGIESLR-ATTRDIPD----YDVLMKQRLRiLDEHGLKLSDIQEVIAT-LKPLEGAV 74
Cdd:TIGR01488   1 LAIFDFDGTLTRQdsLIDLLAKLLGTNDEViELTRLAPSgrisFEDALGRRLA-LLHRSRSEEVAKEFLARqVALRPGAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352543   75 EFVNWLRER-FQVVILSDTFYEFSQPLMRQLGFPTLLCHRLITDETGRVVSYQLRQKDPKRQS-VLAFKSLY-------Y 145
Cdd:TIGR01488  80 ELISWLKERgIDTVIVSGGFDFFVEPVAEKLGIDDVFANRLEFDDNGLLTGPIEGQVNPEGECkGKVLKELLeeskitlK 159

                         170
                  ....*....|....*
gi 966352543  146 RIIAAGDSYNDTTML 160
Cdd:TIGR01488 160 KIIAVGDSVNDLPML 174
HAD_PSP_eu cd04309
phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase; Human ...
 2-178 2.67e-08

phosphoserine phosphatase eukaryotic-like, similar to human phosphoserine phosphatase; Human PSP, EC 3.1.3.3, catalyzes the third and final of the L-serine biosynthesis pathway, the Mg2+-dependent hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, L-serine is a precursor for the biosynthesis of glycine. HPSP regulates the levels of glycine and D-serine (converted from L-serine), the putative co-agonists for the glycine site of the NMDA receptor in the brain. Plant 3-PSP catalyzes the conversion of 3-phosphoserine to serine in the last step of the plastidic pathway of serine biosynthesis. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319801 [Multi-domain]  Cd Length: 202  Bit Score: 51.90  E-value: 2.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352543   2 EIACLDLEGVLVPEIWI-AFAEKTGIES-LRATTR-----DIPDYDVLmKQRLRILDehgLKLSDIQEVIATLKPL--EG 72
Cdd:cd04309    1 DAVCFDVDSTVIQEEGIdELAKFCGVGDeVAELTRramggSIPFRDAL-RKRLAIIN---PTKEQVDEFLEEHPPRltPG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352543  73 AVEFVNWLRER-FQVVILSDTFYEFSQPLMRQLGFPT--LLCHRLITDETGRVVSYQ----LRQKDPKRQSVLAFKSL-- 143
Cdd:cd04309   77 VEELVSRLKARgVEVYLISGGFRELIEPVASQLGIPLenVFANRLLFDFNGEYAGFDetqpTSRSGGKAKVIEQLKEKhh 156

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 966352543 144 YYRIIAAGDSYNDTTMLGEADAGILFHApdNVIRE 178
Cdd:cd04309  157 YKRVIMIGDGATDLEACPPADAFIGFGG--NVIRE 189
Hydrolase pfam00702
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ...
 13-164 9.25e-08

haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha/beta hydrolase family (pfam00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain. Those members with the characteriztic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria.


Pssm-ID: 459910 [Multi-domain]  Cd Length: 191  Bit Score: 50.28  E-value: 9.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352543   13 VPEIWIAFAEKTGIESLRATTRDIPDYDVLMKQRLRILDEHGLKLSDIQEVIATLKPLEGAVEFVNWLRER-FQVVILSD 91
Cdd:pfam00702  43 LPIPVEDFTARLLLGKRDWLEELDILRGLVETLEAEGLTVVLVELLGVIALADELKLYPGAAEALKALKERgIKVAILTG 122

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966352543   92 TFYEFSQPLMRQLGFPTLLCHRLITDETGRvvsyqlrqKDPKRQSVLA----FKSLYYRIIAAGDSYNDTTMLGEAD 164
Cdd:pfam00702 123 DNPEAAEALLRLLGLDDYFDVVISGDDVGV--------GKPKPEIYLAalerLGVKPEEVLMVGDGVNDIPAAKAAG 191
HAD pfam12710
haloacid dehalogenase-like hydrolase;
4-160 2.02e-07

haloacid dehalogenase-like hydrolase;


Pssm-ID: 432733 [Multi-domain]  Cd Length: 188  Bit Score: 49.07  E-value: 2.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352543    4 ACLDLEGVLVP----EIWIAFAEKTGIESLRATTRDIPdYDVLMKQRLRILDEH----------GLKLSDIQEV------ 63
Cdd:pfam12710   1 ALFDLDGTLLDgdslFLLIRALLRRGGPDLWRALLVLL-LLALLRLLGRLSRAGarellrallaGLPEEDAAELerfvae 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352543   64 IATLKPLEGAVEFVNWLRER-FQVVILSDTFYEFSQPLMRQLGFPTLLCHRLITDE---TGRVVSYQL----RQKDPKRQ 135
Cdd:pfam12710  80 VALPRLHPGALELLAAHRAAgDRVVVVTGGLRPLVEPVLAELGFDEVLATELEVDDgrfTGELRLIGPpcagEGKVRRLR 159

                         170       180
                  ....*....|....*....|....*...
gi 966352543  136 SVLAFKSL---YYRIIAAGDSYNDTTML 160
Cdd:pfam12710 160 AWLAARGLgldLADSVAYGDSPSDLPML 187
HAD_PGPPase cd02612
phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 ...
 7-160 4.11e-06

phosphatidylglycerol-phosphate phosphatase, similar to Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C; This family includes Escherichia coli K-12 phosphatidylglycerol-phosphate phosphatase C, PgpC (previously named yfhB) which catalyzes the dephosphorylation of phosphatidylglycerol-phosphate (PGP) to phosphatidylglycerol (PG). This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319796 [Multi-domain]  Cd Length: 195  Bit Score: 45.37  E-value: 4.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352543   7 DLEGVLVP-EIWIAFAEKTGIESLRATTRDIPDYDVL------------MKQRLRILDEHGLKLSDIQE---VIATLKPL 70
Cdd:cd02612    5 DLDGTLIAgDSFFAFLRFKGIAERRAPLEELLLLRLMalyalgrldgagMEALLGFATAGLAGELAALVeefVEEYILRV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352543  71 --EGAVEFVNWLRER-FQVVILSDTFYEFSQPLMRQLGFPTLLCHRLITDE---TGRVVSYQLRQKD-PKR-QSVLAFKS 142
Cdd:cd02612   85 lyPEARELIAWHKAAgHDVVLISASPEELVAPIARKLGIDNVLGTQLETEDgryTGRIIGPPCYGEGkVKRlREWLAEEG 164

                        170
                 ....*....|....*....
gi 966352543 143 LYYRIIAA-GDSYNDTTML 160
Cdd:cd02612  165 IDLKDSYAySDSINDLPML 183
HAD_like cd01427
Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily ...
 73-171 1.16e-05

Haloacid dehalogenase-like hydrolases; The haloacid dehalogenase-like (HAD) superfamily includes L-2-haloacid dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, and many others. This superfamily includes a variety of enzymes that catalyze the cleavage of substrate C-Cl, P-C, and P-OP bonds via nucleophilic substitution pathways. All of which use a nucleophilic aspartate in their phosphoryl transfer reaction. They catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. Members of this superfamily are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319763 [Multi-domain]  Cd Length: 106  Bit Score: 42.77  E-value: 1.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352543  73 AVEFVNWLRER-FQVVILSDTFYEFSQPLMRQLGFPTLLCHRLITDETGRvvsyqlRQKDPKRQSVLAFKSLYY--RIIA 149
Cdd:cd01427   12 AVELLKRLRAAgIKLAIVTNRSREALRALLEKLGLGDLFDGIIGSDGGGT------PKPKPKPLLLLLLKLGVDpeEVLF 85

                         90       100
                 ....*....|....*....|..
gi 966352543 150 AGDSYNDTTMLgeADAGILFHA 171
Cdd:cd01427   86 VGDSENDIEAA--RAAGGRTVA 105
YcjU COG0637
Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];
7-83 3.08e-03

Beta-phosphoglucomutase, HAD superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 440402 [Multi-domain]  Cd Length: 208  Bit Score: 37.11  E-value: 3.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352543   7 DLEGVLVP------EIWIAFAEKTGIESLRATTRDI---PDYDVLMkqrlRILDEHGLKLSD----------IQEVIAT- 66
Cdd:COG0637    8 DMDGTLVDseplhaRAWREAFAELGIDLTEEEYRRLmgrSREDILR----YLLEEYGLDLPEeelaarkeelYRELLAEe 83

                         90
                 ....*....|....*...
gi 966352543  67 -LKPLEGAVEFVNWLRER 83
Cdd:COG0637   84 gLPLIPGVVELLEALKEA 101
YigB COG1011
FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily ...
 48-121 9.73e-03

FMN and 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB, HAD superfamily (riboflavin biosynthesis) [Coenzyme transport and metabolism];


Pssm-ID: 440635 [Multi-domain]  Cd Length: 220  Bit Score: 35.77  E-value: 9.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966352543  48 RILDEHGLKLSD------IQEVIATLKPLEGAVEFVNWLRER-FQVVILSDTFYEFSQPLMRQLGFPTLLCHRLITDETG 120
Cdd:COG1011   67 RLLEELGLDLAEelaeafLAALPELVEPYPDALELLEALKARgYRLALLTNGSAELQEAKLRRLGLDDLFDAVVSSEEVG 146


                 .
gi 966352543 121 R 121
Cdd:COG1011  147 V 147
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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